ArticleJournal of the American Chemical Society2026
Interface Architecture of a VHL-PROTAC Complex with and without Cullin-2.
Article in Journal of the American Chemical Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
2 citing papers in PubMed.
- Native Mass Spectrometry Analysis of Cullin-RING Ubiquitin E3 Ligase Complexes in the Context of Targeted Protein Degradation.Analytical chemistry · 2026Article
- Interface Architecture of a VHL-PROTAC Complex with and without Cullin-2.Journal of the American Chemical Society · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
Proteolysis Targeting Chimeras (PROTACs) are bispecific molecules that link a target protein to an E3 ligase, leading to ubiquitination and subsequent degradation. Their efficacy depends on their ability to form ternary complexes for target ubiquitination, which is influenced by protein-protein interactions. Native mass spectrometry combined with surface-induced dissociation (SID) is a sensitive technique for rapidly assessing protein structures, including stoichiometry and interfacial strengths. Native mass spectrometry can also capture a variety of conformational states in the gas phase, reflecting the intrinsic flexibility of many protein assemblies. This ability to resolve structural heterogeneity and transient subpopulations provides complementary insights not as readily accessible through crystallography, cryo-EM, or other ensemble-averaging assays. By coupling native mass spectrometry with surface-induced dissociation, topological features, specifically relative interfacial strengths and subcomplex arrangements, were probed
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Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.